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Title: Emerging evidence for kindlin oligomerization and its role in regulating kindlin function
Authors: Bu, Wenting
Levitskaya, Zarina
Tan, Suet-Mien
Gao, Yong-Gui
Keywords: Science::Biological sciences
Issue Date: 2021
Source: Bu, W., Levitskaya, Z., Tan, S. & Gao, Y. (2021). Emerging evidence for kindlin oligomerization and its role in regulating kindlin function. Journal of Cell Science, 134(8), jcs256115-.
Project: MOE2017-T2-1-106
Journal: Journal of Cell Science
Abstract: Integrin-mediated cell-extracellular matrix (ECM) interactions play crucial roles in a broad range of physiological and pathological processes. Kindlins are important positive regulators of integrin activation. The FERM-domain-containing kindlin family comprises three members, kindlin-1, kindlin-2 and kindlin-3 (also known as FERMT1, FERMT2 and FERMT3), which share high sequence similarity (identity >50%), as well as domain organization, but exhibit diverse tissue-specific expression patterns and cellular functions. Given the significance of kindlins, analysis of their atomic structures has been an attractive field for decades. Recently, the structures of kindlin and its β-integrin-bound form have been obtained, which greatly advance our understanding of the molecular functions that involve kindlins. In particular, emerging evidence indicates that oligomerization of kindlins might affect their integrin binding and focal adhesion localization, positively or negatively. In this Review, we presented an update on the recent progress of obtaining kindlin structures, and discuss the implication for integrin activation based on kindlin oligomerization, as well as the possible regulation of this process.
ISSN: 0021-9533
DOI: 10.1242/jcs.256115
Schools: School of Biological Sciences 
Research Centres: NTU Institute of Structural Biology 
Rights: © 2021 The Author(s). All rights reserved. This paper was published by The Company of Biologists Ltd in Journal of Cell Science and is made available with permission of The Author(s).
Fulltext Permission: open
Fulltext Availability: With Fulltext
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